6NJG: Ubiquitin Variant

Ubiquitin Variant in Complex with Ubiquitin Interacting Motif. Determined by X-ray diffraction at 2.35 Å resolution. Released 6 Mar 2019.

Method
X-ray diffraction
Resolution
2.35 Å
Organisms
Saccharomyces cerevisiae (strain ATCC 204508 / S288c), Homo sapiens
Chains
2
Atoms
726
Mol. weight
12.57 kDa
Released
6 Mar 2019

Explore 6NJG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6NJG contains 5 α-helices and 5 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain B: 1 helix, 0 β-strands

ElementResiduesLengthSheet
α-helix1-1414
Chain C: 4 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand2211
α-helix23-3412
α-helix38-403
β-strand41-4552
β-strand48-4922
α-helix50-512
β-strand5511
α-helix57-593
β-strand68-7142

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Vacuolar protein sorting-associated protein 27Bprotein24Saccharomyces cerevisiae (strain ATCC 204508 / S288c)P40343 (AlphaFold model)
Polyubiquitin-BCprotein89Homo sapiensJ3QS39 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>6NJG_1 Vacuolar protein sorting-associated protein 27 (chains B)
YPEDEEELIRKAIELSLKESRNSA
Sequence of entity 2 (C), FASTA
>6NJG_2 Polyubiquitin-B (chains C)
GGAAQPAMQIFVQTITVMRIALEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGMQLEDG
RTLSDYNIKRDSNLYLVSSLRSLRAGAAA

Primary citation

Dimerization of a ubiquitin variant leads to high affinity interactions with a ubiquitin interacting motif. Manczyk, N., Veggiani, G., Gish, G.D. et al. Protein Sci (2019) 28:848-856. DOI 10.1002/pro.3593 · PubMed

Other PDB entries of the same protein (UniProt P40343 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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